4j33

X-ray diffraction
1.82Å resolution

Crystal Structure of kynurenine 3-monooxygenase (KMO-394)

Released:

Function and Biology Details

Reaction catalysed:
L-kynurenine + NADPH + O(2) = 3-hydroxy-L-kynurenine + NADP(+) + H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-153562 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kynurenine 3-monooxygenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 415 amino acids
Theoretical weight: 47.05 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Not provided
UniProt:
  • Canonical: P38169 (Residues: 1-394; Coverage: 86%)
Gene names: BNA4, YBL0828, YBL098W
Sequence domains: FAD binding domain
Structure domains: FAD/NAD(P)-binding domain

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P21
Unit cell:
a: 58.43Å b: 98.73Å c: 85.42Å
α: 90° β: 105.26° γ: 90°
R-values:
R R work R free
0.189 0.187 0.222
Expression system: Not provided